Effect of Hofmeister series anions on freeze-thaw stability of emulsion stabilized with whey protein isolates

• Published in: Food hydrocolloids 2023-01, Vol.134, p.108015, Article 108015
• Main Authors: Lai, Hao, Shen, Qian, Zhan, Fuchao, Jiang, Sha, Sui, Haomin, Chen, Yijie, Li, Bin, Li, Jing
• Format: Article
• Language: English
• Subjects: Emulsion; Freeze-thaw stability; Hofmeister series anions; Whey protein isolates
• ISSN: 0268-005X; 1873-7137
• DOI: 10.1016/j.foodhyd.2022.108015

The effect of Hofmeister series anions at different concentrations on the freeze-thaw (FT) stability of emulsions stabilized with whey protein isolate (WPI) and its possible mechanism were studied. The emulsions prepared from WPI added with kosmotropic ions (Cl− and Br−) presented good freeze-thaw stability, whereas those without NaCl were destabilized after freeze-thawing. In addition, the adsorbed protein (AP) percentage, protein load (τ), apparent viscosity, and mechanical moduli of emulsions added with Cl− and Br− were increased with the salt addition, thus facilitating the formation of elastic gel network structure in the emulsion system. WPI added with NaCl exhibited high interfacial pressure (π) and diffusion rate (Kdiff), indicating that its interfacial behavior promoted the stability of oil-water interface. During the adsorption process, the relative abundance of transferrin (TRF) and immunoglobulin (Ig) of WPI was increased, suggesting their higher interfacial affinity at the interface. After three FT cycles of the emulsion prepared from WPI added with Cl−, the proteins with low molecular weight (LMW) presented better emulsification activity. The decreased relative abundance of TRF and Ig due to the extrusion of the ice crystals would be responsible for the instability of the WPI-stabilized emulsion by freeze-thaw treatment. [Display omitted] •WPI emulsions with Cl− and Br− addition exhibited good freeze-thaw (FT) stability.•The addition of kosmotropic ions increased the surface hydrophobicity of protein.•The surface hydrophobicity of protein with chaotropic ions was decreased.•Relative abundance of low-molecular-weight protein increased after three FT cycles.•Proteins with more quantities at the interface suggested the preferential adsorption.